PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30962087-1	2019	A series of DNA gyrase inhibitors were designed based on the X-ray structure of a parent thiophene scaffold with the objective to improve biochemical and whole-cell antibacterial activity, while reducing cardiac ion channel activity.	Thiophenes	89-98	DNA topoisomerase II alpha	Homo sapiens	12-22	
28507124-0	2017	Thiophene antibacterials that allosterically stabilize DNA-cleavage complexes with DNA gyrase.	Thiophenes	0-9	DNA topoisomerase II alpha	Homo sapiens	83-93	
28507124-3	2017	We have identified a class of antibacterial thiophenes that target DNA gyrase with a unique mechanism of action and have activity against a range of bacterial pathogens, including strains resistant to fluoroquinolones.	Thiophenes	44-54	DNA topoisomerase II alpha	Homo sapiens	67-77	
28507124-6	2017	Mutations of conserved residues around this pocket affect activity of the thiophene inhibitors, consistent with allosteric inhibition of DNA gyrase.	Thiophenes	74-83	DNA topoisomerase II alpha	Homo sapiens	137-147